CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022211
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Fanconi anemia group I protein 
Protein Synonyms/Alias
 Protein FACI 
Gene Name
 FANCI 
Gene Synonyms/Alias
 KIAA1794 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
4****MDQKILSLAAEubiquitination[1, 2, 3, 4]
12ILSLAAEKTADKLQEubiquitination[3, 5]
16AAEKTADKLQEFLQTubiquitination[1, 3, 4, 5]
39LLQNQAVKGKVAGALubiquitination[1, 2, 3, 4, 5, 6, 7]
41QNQAVKGKVAGALLRubiquitination[2, 3]
52ALLRAIFKGSPCSEEubiquitination[1, 2, 3, 4]
125EGSLVNGKSLELLPIubiquitination[3]
140ILTALATKKENLAYGubiquitination[7]
141LTALATKKENLAYGKubiquitination[3]
148KENLAYGKGVLSGEEubiquitination[3]
157VLSGEECKKQLINTLubiquitination[3]
158LSGEECKKQLINTLCubiquitination[3]
331DQVLDLLKTSVVKSFubiquitination[3, 5, 7]
336LLKTSVVKSFKDLQLubiquitination[1, 4, 5]
339TSVVKSFKDLQLLQGubiquitination[1, 3, 4, 5]
348LQLLQGSKFLQNLVPubiquitination[1, 3, 4, 5]
402PKKVLDGKTIETSPSubiquitination[1, 2, 3, 4, 5, 7]
420MPNQHACKLGANILLubiquitination[3]
431NILLETFKIHEMIRQubiquitination[3]
501QTVQRLLKAVQPLLKubiquitination[1, 3, 4, 5, 7]
508KAVQPLLKVSMSMRDubiquitination[5]
523CLILVLRKAMFANQLubiquitination[1, 3, 4, 5, 7, 8]
638LKQFYEPKPDLLPPLubiquitination[1, 4, 5]
715SITNRMIKSELEDFEubiquitination[1, 3, 4, 5, 7]
725LEDFELDKSADFSQSubiquitination[5]
780SLFMCYKKLSDILNEubiquitination[3]
788LSDILNEKAGKAKTKubiquitination[3, 5]
799AKTKMANKTSDSLLSubiquitination[3]
849AVNVALQKVQQLKETubiquitination[1, 2, 3, 4, 5, 6, 7, 9, 10]
854LQKVQQLKETGHVSGubiquitination[3, 5, 7, 9, 10]
869PDGQNPEKIFQNLCDubiquitination[3, 9]
897TSVEESGKKEKGKSIubiquitination[5, 7]
898SVEESGKKEKGKSISubiquitination[3]
900EESGKKEKGKSISLLubiquitination[3]
902SGKKEKGKSISLLCLubiquitination[2, 3]
926VQQFYQPKIQQFLRAubiquitination[3, 6]
939RALDVTDKEGEEREDubiquitination[3, 5]
1015SWTSKICKENSREDAubiquitination[3]
1068DQDVEVEKTNHFAIVubiquitination[3, 5]
1105EVDWLITKLKGQVSQubiquitination[1, 4, 5, 7]
1107DWLITKLKGQVSQETubiquitination[3, 5, 7, 9, 10]
1196GIPKNMEKLVKLSGSubiquitination[3]
1199KNMEKLVKLSGSHLTubiquitination[3]
1221SYVQNKSKSLNYTGEubiquitination[1, 3, 4, 5]
1230LNYTGEKKEKPAAVAubiquitination[2, 3]
1232YTGEKKEKPAAVATAubiquitination[2, 3]
1248ARVLRETKPIPNLIFubiquitination[3, 5]
1269KFLIHLSKKSKVNLMubiquitination[3]
1270FLIHLSKKSKVNLMQubiquitination[3]
1272IHLSKKSKVNLMQHMubiquitination[3]
1280VNLMQHMKLSTSRDFubiquitination[3]
1290TSRDFKIKGNILDMVubiquitination[3]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [5] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [6] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [7] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [8] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [9] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [10] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
Functional Description
 Plays an essential role in the repair of DNA double- strand breaks by homologous recombination and in the repair of interstrand DNA cross-links (ICLs) by promoting FANCD2 monoubiquitination by FANCL and participating in recruitment to DNA repair sites. Required for maintenance of chromosomal stability. Specifically binds branched DNA: binds both single- stranded DNA (ssDNA) and double-stranded DNA (dsDNA). Participates in S phase and G2 phase checkpoint activation upon DNA damage. 
Sequence Annotation
 MOD_RES 407 407 Phosphoserine.
 MOD_RES 556 556 Phosphoserine (By similarity).
 MOD_RES 730 730 Phosphoserine.
 MOD_RES 952 952 Phosphothreonine.
 MOD_RES 1121 1121 Phosphoserine.
 CROSSLNK 523 523 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Alternative splicing; Cell cycle; Complete proteome; Direct protein sequencing; Disease mutation; DNA damage; DNA repair; DNA-binding; Fanconi anemia; Isopeptide bond; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1328 AA 
Protein Sequence
MDQKILSLAA EKTADKLQEF LQTLREGDLT NLLQNQAVKG KVAGALLRAI FKGSPCSEEA 60
GTLRRRKIYT CCIQLVESGD LQKEIASEII GLLMLEAHHF PGPLLVELAN EFISAVREGS 120
LVNGKSLELL PIILTALATK KENLAYGKGV LSGEECKKQL INTLCSGRWD QQYVIQLTSM 180
FKDVPLTAEE VEFVVEKALS MFSKMNLQEI PPLVYQLLVL SSKGSRKSVL EGIIAFFSAL 240
DKQHNEEQSG DELLDVVTVP SGELRHVEGT IILHIVFAIK LDYELGRELV KHLKVGQQGD 300
SNNNLSPFSI ALLLSVTRIQ RFQDQVLDLL KTSVVKSFKD LQLLQGSKFL QNLVPHRSYV 360
STMILEVVKN SVHSWDHVTQ GLVELGFILM DSYGPKKVLD GKTIETSPSL SRMPNQHACK 420
LGANILLETF KIHEMIRQEI LEQVLNRVVT RASSPISHFL DLLSNIVMYA PLVLQSCSSK 480
VTEAFDYLSF LPLQTVQRLL KAVQPLLKVS MSMRDCLILV LRKAMFANQL DARKSAVAGF 540
LLLLKNFKVL GSLSSSQCSQ SLSVSQVHVD VHSHYNSVAN ETFCLEIMDS LRRCLSQQAD 600
VRLMLYEGFY DVLRRNSQLA NSVMQTLLSQ LKQFYEPKPD LLPPLKLEAC ILTQGDKISL 660
QEPLDYLLCC IQHCLAWYKN TVIPLQQGEE EEEEEEAFYE DLDDILESIT NRMIKSELED 720
FELDKSADFS QSTSIGIKNN ICAFLVMGVC EVLIEYNFSI SSFSKNRFED ILSLFMCYKK 780
LSDILNEKAG KAKTKMANKT SDSLLSMKFV SSLLTALFRD SIQSHQESLS VLRSSNEFMR 840
YAVNVALQKV QQLKETGHVS GPDGQNPEKI FQNLCDITRV LLWRYTSIPT SVEESGKKEK 900
GKSISLLCLE GLQKIFSAVQ QFYQPKIQQF LRALDVTDKE GEEREDADVS VTQRTAFQIR 960
QFQRSLLNLL SSQEEDFNSK EALLLVTVLT SLSKLLEPSS PQFVQMLSWT SKICKENSRE 1020
DALFCKSLMN LLFSLHVSYK SPVILLRDLS QDIHGHLGDI DQDVEVEKTN HFAIVNLRTA 1080
APTVCLLVLS QAEKVLEEVD WLITKLKGQV SQETLSEEAS SQATLPNQPV EKAIIMQLGT 1140
LLTFFHELVQ TALPSGSCVD TLLKDLCKMY TTLTALVRYY LQVCQSSGGI PKNMEKLVKL 1200
SGSHLTPLCY SFISYVQNKS KSLNYTGEKK EKPAAVATAM ARVLRETKPI PNLIFAIEQY 1260
EKFLIHLSKK SKVNLMQHMK LSTSRDFKIK GNILDMVLRE DGEDENEEGT ASEHGGQNKE 1320
PAKKKRKK 1328 
Gene Ontology
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0006281; P:DNA repair; TAS:Reactome.
 GO:0031398; P:positive regulation of protein ubiquitination; IDA:MGI. 
Interpro
 IPR026171; FANCI. 
Pfam
  
SMART
  
PROSITE
  
PRINTS